사독 arginine-sterase투여가 인체의 엽록소 용해력에 미치는 영향
- Alternative Title
- Effect of Snake Venom : Arginine-esterase on the Fibrinolytic Activity
- Abstract
- Background and purpose: Arginine esterase(Ancrod), a thrombin-like enzyme, purified from the venoms of Agkistrodon halys, has known to cleave fibrinopeptide A from the fibrinogen and lead to circulation of soluble noncross-linked ""ancrodfibrin', which stimulates endogenous T-PA release. Many authors have suggested clinical applicability of this enzyme,but clinical studies on its fibrinolytic action has been insufficient.Thus we studied the influence of this enzyme on fibrinolytic activity in cerebral infarction.
Method: We observed the change of euglobulin fibrinolytic activity, t-PA antigen, t-PA activity, fibrinopeptide A, fibrinogen, FDP and D-dimer, during 12 hours after a bolus intravenous administration of 0.25 unit of the arginine esterase to the 9 patients with cerebral infarction.
Result: There was no change of the euglobulin fibrinolytic activity, fibrinopeptide A and t-PA Ag but there was significant increase in both t-PA activity and FDP, D-dimer and significant decrease in fibrinogen.
Conclusion: Our result suggest that arginine esterase converts fibrinogen to a fibrin polymer which has a increased susceptibility to lysis by plasmirl This enzyme seems to amplify T-PA activity through the consequent increase in FT)P, because there is no increase in the euglobulin fibrinolytic activity, fibr'mopeptide A and t-PA Ag suggesting direct T-PA release. Arginine esterase, having action of effective defibrinogenation and safe fibrinolysis,could be used for the thrombus related disease.
- All Author(s)
- J. M. Park
; J. W. Lim
; H. K. Park
; K. B. Sung
; M. Y. Ahn
; H. K. Shin
- Intsitutional Author(s)
- 박형국
- Issued Date
- 1995
- Type
- Article
- Publisher
- 대한신경과학회
Korean Neurological Association
- ISSN
- 1225-7044
; 2288-985X
- Citation Title
- 대한신경과학회지
Journal of the Korean Neurological Association
- Citation Volume
- 13
- Citation Number
- 3
- Citation Start Page
- 464
- Citation End Page
- 472
- Language(ISO)
- kor
- URI
- http://schca-ir.schmc.ac.kr/handle/2022.oak/4013
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